PFD5_HUMAN
ID PFD5_HUMAN Reviewed; 154 AA.
AC Q99471; A8K9A8; Q54AA8; Q9C083; Q9C084;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Prefoldin subunit 5;
DE AltName: Full=Myc modulator 1;
DE AltName: Full=c-Myc-binding protein Mm-1;
GN Name=PFDN5; Synonyms=MM1, PFD5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9792694; DOI=10.1074/jbc.273.45.29794;
RA Mori K., Maeda Y., Kitaura H., Taira T., Iguchi-Ariga S.M., Ariga H.;
RT "MM-1, a novel c-Myc-associating protein that represses transcriptional
RT activity of c-Myc.";
RL J. Biol. Chem. 273:29794-29800(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Blood, and Fibroblast;
RX PubMed=11567024; DOI=10.1074/jbc.m106127200;
RA Fujioka Y., Taira T., Maeda Y., Tanaka S., Nishihara H.,
RA Iguchi-Ariga S.M.M., Nagashima K., Ariga H.;
RT "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in
RT leukemia/lymphoma and tongue cancer.";
RL J. Biol. Chem. 276:45137-45144(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RC TISSUE=B-cell, and Placenta;
RX PubMed=16173081; DOI=10.1002/jcb.20619;
RA Hagio Y., Kimura Y., Taira T., Fujioka Y., Iguchi-Ariga S.M.M., Ariga H.;
RT "Distinct localizations and repression activities of MM-1 isoforms toward
RT c-Myc.";
RL J. Cell. Biochem. 97:145-155(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION.
RX PubMed=9630229; DOI=10.1016/s0092-8674(00)81446-4;
RA Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J.,
RA Klein H.L., Cowan N.J.;
RT "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
RT chaperonin.";
RL Cell 93:863-873(1998).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC transfers target proteins to it. Binds to nascent polypeptide chain and
CC promotes folding in an environment in which there are many competing
CC pathways for nonnative proteins. Represses the transcriptional activity
CC of MYC. {ECO:0000269|PubMed:9630229}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits. Binds to MYC; interacts with its N-terminal domain.
CC -!- INTERACTION:
CC Q99471; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-357275, EBI-11096309;
CC Q99471; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-357275, EBI-14493093;
CC Q99471; O75934: BCAS2; NbExp=3; IntAct=EBI-357275, EBI-1050106;
CC Q99471; P41182: BCL6; NbExp=3; IntAct=EBI-357275, EBI-765407;
CC Q99471; O14503: BHLHE40; NbExp=3; IntAct=EBI-357275, EBI-711810;
CC Q99471; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-357275, EBI-12809220;
CC Q99471; Q5T681: C10orf62; NbExp=3; IntAct=EBI-357275, EBI-744052;
CC Q99471; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-357275, EBI-12155483;
CC Q99471; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-357275, EBI-7317823;
CC Q99471; Q96LM5: C4orf45; NbExp=3; IntAct=EBI-357275, EBI-12020542;
CC Q99471; Q8N865: C7orf31; NbExp=3; IntAct=EBI-357275, EBI-10174456;
CC Q99471; Q13137: CALCOCO2; NbExp=4; IntAct=EBI-357275, EBI-739580;
CC Q99471; E9PSE9: CCDC198; NbExp=3; IntAct=EBI-357275, EBI-11748295;
CC Q99471; Q1MSJ5-1: CSPP1; NbExp=3; IntAct=EBI-357275, EBI-10239122;
CC Q99471; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-357275, EBI-9679045;
CC Q99471; Q8TEW6: DOK4; NbExp=3; IntAct=EBI-357275, EBI-6918542;
CC Q99471; Q9P104-2: DOK5; NbExp=3; IntAct=EBI-357275, EBI-10692909;
CC Q99471; P41970: ELK3; NbExp=3; IntAct=EBI-357275, EBI-1758534;
CC Q99471; Q6ZVH7: ESPNL; NbExp=3; IntAct=EBI-357275, EBI-12831272;
CC Q99471; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-357275, EBI-12013806;
CC Q99471; Q5T9C2-3: FAM102A; NbExp=3; IntAct=EBI-357275, EBI-11980989;
CC Q99471; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-357275, EBI-1752811;
CC Q99471; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-357275, EBI-745689;
CC Q99471; A4D161: FAM221A; NbExp=3; IntAct=EBI-357275, EBI-11960181;
CC Q99471; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-357275, EBI-2807642;
CC Q99471; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-357275, EBI-6658203;
CC Q99471; O76003: GLRX3; NbExp=3; IntAct=EBI-357275, EBI-374781;
CC Q99471; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-357275, EBI-748515;
CC Q99471; O95872: GPANK1; NbExp=3; IntAct=EBI-357275, EBI-751540;
CC Q99471; Q9H4Y5: GSTO2; NbExp=3; IntAct=EBI-357275, EBI-10194609;
CC Q99471; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-357275, EBI-11978177;
CC Q99471; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-357275, EBI-11956675;
CC Q99471; Q03014: HHEX; NbExp=3; IntAct=EBI-357275, EBI-747421;
CC Q99471; P17482: HOXB9; NbExp=3; IntAct=EBI-357275, EBI-745290;
CC Q99471; P31273: HOXC8; NbExp=3; IntAct=EBI-357275, EBI-1752118;
CC Q99471; P42858: HTT; NbExp=3; IntAct=EBI-357275, EBI-466029;
CC Q99471; Q9UKT9: IKZF3; NbExp=7; IntAct=EBI-357275, EBI-747204;
CC Q99471; Q14005-2: IL16; NbExp=3; IntAct=EBI-357275, EBI-17178971;
CC Q99471; Q0VD86: INCA1; NbExp=3; IntAct=EBI-357275, EBI-6509505;
CC Q99471; Q9BZI1: IRX2; NbExp=3; IntAct=EBI-357275, EBI-12166369;
CC Q99471; P78412: IRX6; NbExp=3; IntAct=EBI-357275, EBI-12100506;
CC Q99471; Q7L273: KCTD9; NbExp=3; IntAct=EBI-357275, EBI-4397613;
CC Q99471; O60341: KDM1A; NbExp=3; IntAct=EBI-357275, EBI-710124;
CC Q99471; O14901: KLF11; NbExp=3; IntAct=EBI-357275, EBI-948266;
CC Q99471; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-357275, EBI-6426443;
CC Q99471; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-357275, EBI-739890;
CC Q99471; Q6P4E2: LARP4; NbExp=3; IntAct=EBI-357275, EBI-12079790;
CC Q99471; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-357275, EBI-739832;
CC Q99471; Q13163: MAP2K5; NbExp=3; IntAct=EBI-357275, EBI-307294;
CC Q99471; Q8WXB1: METTL21A; NbExp=3; IntAct=EBI-357275, EBI-8652459;
CC Q99471; Q8IVT2: MISP; NbExp=3; IntAct=EBI-357275, EBI-2555085;
CC Q99471; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-357275, EBI-2514313;
CC Q99471; Q9UBF9: MYOT; NbExp=3; IntAct=EBI-357275, EBI-296701;
CC Q99471; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-357275, EBI-744402;
CC Q99471; Q9H2A3: NEUROG2; NbExp=3; IntAct=EBI-357275, EBI-7969348;
CC Q99471; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-357275, EBI-12025760;
CC Q99471; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-357275, EBI-741158;
CC Q99471; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-357275, EBI-11022007;
CC Q99471; P55771: PAX9; NbExp=3; IntAct=EBI-357275, EBI-12111000;
CC Q99471; Q7Z412: PEX26; NbExp=3; IntAct=EBI-357275, EBI-752057;
CC Q99471; Q9UHV9: PFDN2; NbExp=5; IntAct=EBI-357275, EBI-359873;
CC Q99471; O43189: PHF1; NbExp=3; IntAct=EBI-357275, EBI-530034;
CC Q99471; Q9UPV7: PHF24; NbExp=3; IntAct=EBI-357275, EBI-17717171;
CC Q99471; C9JJ79: PILRA; NbExp=3; IntAct=EBI-357275, EBI-12117156;
CC Q99471; P78337: PITX1; NbExp=3; IntAct=EBI-357275, EBI-748265;
CC Q99471; Q99697-2: PITX2; NbExp=3; IntAct=EBI-357275, EBI-12138495;
CC Q99471; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-357275, EBI-1389308;
CC Q99471; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-357275, EBI-12000762;
CC Q99471; O43741: PRKAB2; NbExp=3; IntAct=EBI-357275, EBI-1053424;
CC Q99471; Q99633: PRPF18; NbExp=3; IntAct=EBI-357275, EBI-2798416;
CC Q99471; P0CG20: PRR35; NbExp=3; IntAct=EBI-357275, EBI-11986293;
CC Q99471; P28070: PSMB4; NbExp=3; IntAct=EBI-357275, EBI-603350;
CC Q99471; P28062-2: PSMB8; NbExp=3; IntAct=EBI-357275, EBI-372312;
CC Q99471; P61289: PSME3; NbExp=6; IntAct=EBI-357275, EBI-355546;
CC Q99471; Q8N443: RIBC1; NbExp=3; IntAct=EBI-357275, EBI-10265323;
CC Q99471; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-357275, EBI-10226430;
CC Q99471; Q7L4I2: RSRC2; NbExp=3; IntAct=EBI-357275, EBI-953753;
CC Q99471; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-357275, EBI-6257312;
CC Q99471; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-357275, EBI-3957636;
CC Q99471; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-357275, EBI-748391;
CC Q99471; O00560: SDCBP; NbExp=3; IntAct=EBI-357275, EBI-727004;
CC Q99471; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-357275, EBI-12037847;
CC Q99471; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-357275, EBI-10269374;
CC Q99471; Q8IYB5-2: SMAP1; NbExp=3; IntAct=EBI-357275, EBI-12061577;
CC Q99471; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-357275, EBI-2872322;
CC Q99471; O95863: SNAI1; NbExp=3; IntAct=EBI-357275, EBI-1045459;
CC Q99471; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-357275, EBI-9675976;
CC Q99471; P14678-2: SNRPB; NbExp=3; IntAct=EBI-357275, EBI-372475;
CC Q99471; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-357275, EBI-12288855;
CC Q99471; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-357275, EBI-11959123;
CC Q99471; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-357275, EBI-742688;
CC Q99471; B7ZLI8: STK19; NbExp=3; IntAct=EBI-357275, EBI-10176124;
CC Q99471; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-357275, EBI-745392;
CC Q99471; Q9Y6J9: TAF6L; NbExp=3; IntAct=EBI-357275, EBI-743984;
CC Q99471; O15119: TBX3; NbExp=3; IntAct=EBI-357275, EBI-3452216;
CC Q99471; Q9Y242: TCF19; NbExp=3; IntAct=EBI-357275, EBI-7413767;
CC Q99471; Q92734: TFG; NbExp=3; IntAct=EBI-357275, EBI-357061;
CC Q99471; Q08117-2: TLE5; NbExp=3; IntAct=EBI-357275, EBI-11741437;
CC Q99471; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-357275, EBI-8451480;
CC Q99471; Q9UIW0: VAX2; NbExp=3; IntAct=EBI-357275, EBI-12090999;
CC Q99471; P61758: VBP1; NbExp=7; IntAct=EBI-357275, EBI-357430;
CC Q99471; Q14119: VEZF1; NbExp=3; IntAct=EBI-357275, EBI-11980193;
CC Q99471; Q99990: VGLL1; NbExp=3; IntAct=EBI-357275, EBI-11983165;
CC Q99471; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-357275, EBI-12032042;
CC Q99471; P62699: YPEL5; NbExp=3; IntAct=EBI-357275, EBI-11721624;
CC Q99471; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-357275, EBI-14104088;
CC Q99471; Q9UQR1-2: ZNF148; NbExp=3; IntAct=EBI-357275, EBI-11742222;
CC Q99471; Q9DUN1: vIRF-3; Xeno; NbExp=8; IntAct=EBI-357275, EBI-1647907;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=MM1-alpha;
CC IsoId=Q99471-1; Sequence=Displayed;
CC Name=2; Synonyms=MM1-beta;
CC IsoId=Q99471-2; Sequence=VSP_043104;
CC Name=3; Synonyms=MM1-gamma;
CC IsoId=Q99471-3; Sequence=VSP_043103;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal muscle
CC and moderately in other tissues.
CC -!- MISCELLANEOUS: [Isoform 2]: Does not repress transcription activity of
CC MYC. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA14006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D89667; BAA14006.1; ALT_INIT; mRNA.
DR EMBL; AB055802; BAB32643.1; -; Genomic_DNA.
DR EMBL; AB055803; BAB32644.1; -; mRNA.
DR EMBL; AB055804; BAB32645.1; -; mRNA.
DR EMBL; AB055805; BAB32646.1; -; mRNA.
DR EMBL; BT007195; AAP35859.1; -; mRNA.
DR EMBL; AK292623; BAF85312.1; -; mRNA.
DR EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96683.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96685.1; -; Genomic_DNA.
DR EMBL; BC003373; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC062671; AAH62671.1; -; mRNA.
DR CCDS; CCDS8853.1; -. [Q99471-1]
DR CCDS; CCDS8854.1; -. [Q99471-3]
DR RefSeq; NP_002615.2; NM_002624.3. [Q99471-1]
DR RefSeq; NP_665904.1; NM_145897.2. [Q99471-3]
DR PDB; 6NR8; EM; 7.80 A; 5=11-137.
DR PDB; 6NR9; EM; 8.50 A; 5=11-137.
DR PDB; 6NRB; EM; 8.70 A; 5=11-137.
DR PDB; 6NRC; EM; 8.30 A; 5=11-137.
DR PDB; 6NRD; EM; 8.20 A; 5=11-137.
DR PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR AlphaFoldDB; Q99471; -.
DR SMR; Q99471; -.
DR BioGRID; 111226; 271.
DR ComplexPortal; CPX-6149; Prefoldin co-chaperone complex.
DR CORUM; Q99471; -.
DR DIP; DIP-28155N; -.
DR IntAct; Q99471; 161.
DR MINT; Q99471; -.
DR STRING; 9606.ENSP00000447942; -.
DR GlyGen; Q99471; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99471; -.
DR PhosphoSitePlus; Q99471; -.
DR SwissPalm; Q99471; -.
DR BioMuta; PFDN5; -.
DR DMDM; 12231038; -.
DR OGP; Q99471; -.
DR EPD; Q99471; -.
DR jPOST; Q99471; -.
DR MassIVE; Q99471; -.
DR MaxQB; Q99471; -.
DR PaxDb; Q99471; -.
DR PeptideAtlas; Q99471; -.
DR PRIDE; Q99471; -.
DR ProteomicsDB; 78287; -. [Q99471-1]
DR ProteomicsDB; 78288; -. [Q99471-2]
DR ProteomicsDB; 78289; -. [Q99471-3]
DR TopDownProteomics; Q99471-1; -. [Q99471-1]
DR TopDownProteomics; Q99471-3; -. [Q99471-3]
DR Antibodypedia; 1782; 263 antibodies from 28 providers.
DR DNASU; 5204; -.
DR Ensembl; ENST00000243040.10; ENSP00000243040.6; ENSG00000123349.15. [Q99471-2]
DR Ensembl; ENST00000334478.9; ENSP00000334188.4; ENSG00000123349.15. [Q99471-1]
DR Ensembl; ENST00000351500.7; ENSP00000266964.4; ENSG00000123349.15. [Q99471-3]
DR Ensembl; ENST00000551018.5; ENSP00000447942.1; ENSG00000123349.15. [Q99471-1]
DR GeneID; 5204; -.
DR KEGG; hsa:5204; -.
DR MANE-Select; ENST00000334478.9; ENSP00000334188.4; NM_002624.4; NP_002615.2.
DR UCSC; uc001scl.5; human. [Q99471-1]
DR CTD; 5204; -.
DR DisGeNET; 5204; -.
DR GeneCards; PFDN5; -.
DR HGNC; HGNC:8869; PFDN5.
DR HPA; ENSG00000123349; Low tissue specificity.
DR MIM; 604899; gene.
DR neXtProt; NX_Q99471; -.
DR OpenTargets; ENSG00000123349; -.
DR PharmGKB; PA33210; -.
DR VEuPathDB; HostDB:ENSG00000123349; -.
DR eggNOG; KOG3048; Eukaryota.
DR GeneTree; ENSGT00390000008783; -.
DR HOGENOM; CLU_091867_0_1_1; -.
DR InParanoid; Q99471; -.
DR OMA; QAKFKAC; -.
DR OrthoDB; 1449403at2759; -.
DR PhylomeDB; Q99471; -.
DR TreeFam; TF106509; -.
DR PathwayCommons; Q99471; -.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR SignaLink; Q99471; -.
DR BioGRID-ORCS; 5204; 464 hits in 1091 CRISPR screens.
DR ChiTaRS; PFDN5; human.
DR GeneWiki; PFDN5; -.
DR GenomeRNAi; 5204; -.
DR Pharos; Q99471; Tbio.
DR PRO; PR:Q99471; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q99471; protein.
DR Bgee; ENSG00000123349; Expressed in pituitary gland and 97 other tissues.
DR ExpressionAtlas; Q99471; baseline and differential.
DR Genevisible; Q99471; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0016272; C:prefoldin complex; IDA:FlyBase.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:FlyBase.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0051082; F:unfolded protein binding; IDA:FlyBase.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IDA:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR GO; GO:0006457; P:protein folding; IDA:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR Gene3D; 1.10.287.370; -; 1.
DR HAMAP; MF_00308; PfdA; 1.
DR InterPro; IPR011599; PFD_alpha_archaea.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12674; PTHR12674; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR TIGRFAMs; TIGR00293; TIGR00293; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..154
FT /note="Prefoldin subunit 5"
FT /id="PRO_0000153661"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 25..69
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16173081"
FT /id="VSP_043103"
FT VAR_SEQ 59..154
FT /note="GKELLVPLTSSMYVPGKLHDVEHVLIDVGTGYYVEKTAEDAKDFFKRKIDFL
FT TKQMEKIQPALQEKHAMKQAVMEMMSQKIQQLTALGAAQATAKA -> DVCPWEAA
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16173081"
FT /id="VSP_043104"
SQ SEQUENCE 154 AA; 17328 MW; 0DA1F3644548CB14 CRC64;
MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK
ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA
LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA
